4L1U

Crystal Structure of Human Rtf1 Plus3 Domain in Complex with Spt5 CTR Phosphopeptide

Summary for 4L1U

• Entry DOI: 10.2210/pdb4l1u/pdb
• Related: 4L1P
• Descriptor: RNA polymerase-associated protein RTF1 homolog, Transcription elongation factor SPT5, SULFATE ION, ... (5 entities in total)
• Functional Keywords: tutor, plus3, peptide binding protein, spt5 ctr binding, transcription, paf1 complex, rtf1, orf association region, chromatin, transcription-peptide complex, transcription/peptide
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus, nucleoplasm : Q92541; Nucleus : O00267
• Total number of polymer chains: 10
• Total formula weight: 104562.04

Authors

Wier, A.D.,Heroux, A.,VanDemark, A.P. (deposition date: 2013-06-03, release date: 2013-10-02, Last modification date: 2024-11-06)

Primary citation

Wier, A.D.,Mayekar, M.K.,Heroux, A.,Arndt, K.M.,Vandemark, A.P.
Structural basis for Spt5-mediated recruitment of the Paf1 complex to chromatin.
Proc.Natl.Acad.Sci.USA, 110:17290-17295, 2013

PubMed Abstract: Polymerase associated factor 1 complex (Paf1C) broadly influences gene expression by regulating chromatin structure and the recruitment of RNA-processing factors during transcription elongation. The Plus3 domain of the Rtf1 subunit mediates Paf1C recruitment to genes by binding a repeating domain within the elongation factor Spt5 (suppressor of Ty). Here we provide a molecular description of this interaction by reporting the structure of human Rtf1 Plus3 in complex with a phosphorylated Spt5 repeat. We find that Spt5 binding is mediated by an extended surface containing phosphothreonine recognition and hydrophobic interfaces that interact with residues outside the Spt5 motif. Changes within these interfaces diminish binding of Spt5 in vitro and chromatin localization of Rtf1 in vivo. The structure reveals the basis for recognition of the repeat motif of Spt5, a key player in the recruitment of gene regulatory factors to RNA polymerase II.

PubMed: 24101474
DOI: 10.1073/pnas.1314754110

Experimental method

X-RAY DIFFRACTION (2.424 Å)